1J3M
Crystal structure of the conserved hypothetical protein TT1751 from Thermus thermophilus HB8
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44B2 |
Synchrotron site | SPring-8 |
Beamline | BL44B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-02-04 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9804, 0.9808, 0.9825, 0.9720 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 41.603, 78.811, 44.688 |
Unit cell angles | 90.00, 116.64, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.19694 |
Rwork | 0.194 |
R-free | 0.25884 |
Structure solution method | MAD |
RMSD bond length | 0.024 |
RMSD bond angle | 2.150 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.19) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.036 | 0.138 |
Number of reflections | 16980 | |
<I/σ(I)> | 16.8 | |
Completeness [%] | 97.9 | 83.8 |
Redundancy | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microbatch Crystallization | 5.6 | 293 | PEGMME 5000, Ammonium Sulfate, pH 5.6, Microbatch Crystallization, temperature 293K |